@prefix pubblicazioni: . @prefix unitaDiPersonaleInterno: . @prefix prodotto: . unitaDiPersonaleInterno:MATRICOLA10057 pubblicazioni:autoreCNRDi prodotto:ID11406 . @prefix prodottidellaricerca: . @prefix istituto: . istituto:CDS013 prodottidellaricerca:prodotto prodotto:ID11406 . unitaDiPersonaleInterno:MATRICOLA11582 pubblicazioni:autoreCNRDi prodotto:ID11406 . @prefix modulo: . modulo:ID2527 prodottidellaricerca:prodotto prodotto:ID11406 . @prefix unitaDiPersonaleEsterno: . unitaDiPersonaleEsterno:ID3864 pubblicazioni:autoreCNRDi prodotto:ID11406 . @prefix rdf: . prodotto:ID11406 rdf:type prodotto:TIPO1101 . @prefix retescientifica: . prodotto:ID11406 rdf:type retescientifica:ProdottoDellaRicerca . @prefix rdfs: . prodotto:ID11406 rdfs:label "Unveiling a hidden folding intermediate in c-type cytochromes by protein engineering. (Articolo in rivista)"@en . @prefix xsd: . prodotto:ID11406 pubblicazioni:anno "2006-01-01T00:00:00+01:00"^^xsd:gYear ; pubblicazioni:doi "10.1074/jbc.M512127200"^^xsd:string . @prefix skos: . prodotto:ID11406 skos:altLabel "
Borgia A ., Bonivento D., Travaglini-Allocatelli C., Di Matteo A., Brunori M. (2006)
Unveiling a hidden folding intermediate in c-type cytochromes by protein engineering.
in The Journal of biological chemistry (Print)
"^^rdf:HTML ; pubblicazioni:autori "Borgia A ., Bonivento D., Travaglini-Allocatelli C., Di Matteo A., Brunori M."^^xsd:string ; pubblicazioni:paginaInizio "9331"^^xsd:string ; pubblicazioni:paginaFine "9336"^^xsd:string ; pubblicazioni:numeroVolume "281"^^xsd:string . @prefix ns12: . prodotto:ID11406 pubblicazioni:rivista ns12:ID381209 ; skos:note "ISI Web of Science (WOS)"^^xsd:string ; pubblicazioni:affiliazioni "Univ Roma La Sapienza, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy\nUniv Roma La Sapienza, CNR, Dipartimento Sci Biochim, Ist Biol & Patol Mol, I-00185 Rome, Italy"^^xsd:string ; pubblicazioni:titolo "Unveiling a hidden folding intermediate in c-type cytochromes by protein engineering."^^xsd:string ; prodottidellaricerca:abstract "Several investigators have highlighted a correlation between the basic features of the folding process of a protein and its topology, which dictates the folding pathway. Within this conceptual framework we proposed that different members of the cytochrome c (cyt c) family share the same folding mechanism, involving a consensus partially structured state. Pseudomonas aeruginosa cyt c(551) (Pa cyt c(551)) folds via an apparent two-state mechanism through a high energy intermediate. Here we present kinetic evidence demonstrating that it is possible to switch its folding mechanism from two to three state, stabilizing the high energy intermediate by rational mutagenesis. Characterization of the folding kinetics of one single-site mutant of the Pa cyt c(551) (Phe(7) to Ala) indeed reveals an additional refolding phase and a fast unfolding process which are explained by the accumulation of a partially folded species. Further kinetic analysis highlights the presence of two parallel processes both leading to the native state, suggesting that the above mentioned species is a non obligatory on-pathway intermediate. Determination of the crystallographic structure of F7A shows the presence of an extended internal cavity, which hosts three \\\"bound\\\" water molecules and a H-bond in the N-terminal helix, which is shorter than in the wild type protein. These two features allow us to propose a detailed structural interpretation for the stabilization of the native and especially the intermediate states induced by a single crucial mutation. These results show how protein engineering, x-ray crystallography and state-of-the-art kinetics concur to unveil a folding intermediate and the structural determinants of its stability."@en ; prodottidellaricerca:prodottoDi modulo:ID2527 , istituto:CDS013 ; pubblicazioni:autoreCNR unitaDiPersonaleInterno:MATRICOLA11582 , unitaDiPersonaleEsterno:ID3864 , unitaDiPersonaleInterno:MATRICOLA10057 . ns12:ID381209 pubblicazioni:rivistaDi prodotto:ID11406 .